A PROSS-designed extensively mutated estrogen receptor α variant displays enhanced thermal stability while retaining native allosteric regulation and structure

Abstract Protein stability limitations often hamper the exploration of proteins as drug targets. Here, we show that the application of PROSS server algorithms to the ligand-binding domain of human estrogen receptor alpha (hERα) enabled the development of variant ERPRS* that comprises 24 amino acid s...

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Auteurs principaux: Mark Kriegel, Hanna J. Wiederanders, Sewar Alkhashrom, Jutta Eichler, Yves A. Muller
Format: article
Langue:EN
Publié: Nature Portfolio 2021
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Accès en ligne:https://doaj.org/article/c81ef6036eec4309827b94dcc2a035d3
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